The authors thank the University of Wisconsin-Madison School of Pharmacy Analytical Facility for analytical support. This research was supported in part by National Institutes of Health Grants AI52218 and U19 CA113297.
Probing the Aglycon Promiscuity of an Engineered Glycosyltransferase†
Article first published online: 16 OCT 2008
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 47, Issue 46, pages 8889–8892, November 3, 2008
How to Cite
Gantt, Richard W., Goff, Randal D., Williams, Gavin J. and Thorson, Jon S. (2008), Probing the Aglycon Promiscuity of an Engineered Glycosyltransferase. Angew. Chem. Int. Ed., 47: 8889–8892. doi: 10.1002/anie.200803508
- Issue published online: 28 OCT 2008
- Article first published online: 16 OCT 2008
- Manuscript Received: 18 JUL 2008
- University of Wisconsin-Madison School of Pharmacy Analytical Facility
- National Institutes of Health. Grant Numbers: AI52218, U19 CA113297
- natural products
A sweet library: Two variants (wild-type (WT) and a triple mutant) of glycosyltransferase (GT) OleD have been shown to catalyze glycosylation of over 70 substrates, formation of O-, S- and N-glycosidic bonds, and iterative glycosylation (see scheme). Identified substrates include nucleophiles not previously known to act in GT reactions and span numerous natural product and therapeutic drug classes.